Cashmere-derived keratin for device manufacturing on the micro- and nanoscale

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1 Electronic Supplementary Material (ESI) for Journal of Materials Chemistry C. This journal is The Royal Society of Chemistry 2015 Supporting Information Cashmere-derived keratin for device manufacturing on the micro- and nanoscale Benedetto Marelli and Fiorenzo G. Omenetto* B. Marelli and F. G. Omenetto* Department of Biomedical Engineering Tufts University 4 Colby St., Medford, MA, 02155, USA Fiorenzo.Omenetto@tufts.edu F. G. Omenetto Department of Physics Tufts University 4 Colby St., Medford, MA Keywords: keratin, optic, photonic, sensing 1

2 Experimental details Keratin extraction: Keratin is a family of proteins. Extraction of the proteins that form cashmere fibers yields not a single protein but several proteins, which falls under the name of keratins. For simplicity and clearness to non-technical experts, in the manuscripts we referred to this pool of proteins as keratin, considering it as a single entity. Keratin extraction was performed with a previously reported method 1, with some modifications. In brief, raw, white cashmere wool (30g) was rinse in distilled water (6 liters, 30 C) for 30 minutes (three water changes every 10 minutes), blotted and dried under vacuum for 6 hours. Lipid extraction was then performed with 100% acetone for 24 hours to remove remaining unbound surface lipids. The fibers were then washed (3x) with distilled water (6 liters, 30 C) for 3 hours (three water changes every 45 min) and air-dried. Delipided cashmere fibers were then cut into short fibers, 3 mm long. A mixture of 7M urea (500 ml), 2-mercaptoethanol (50 ml) and 0.5M thiolurea (50 ml), was used to solubilized 30 g of cashmere at 50 C for 72h. The solution was then filtered through a stainless steel sieve (#200) and dialyzed in dialysis tubes (3,500 MW cut-off) against distilled water (8 liters) for 72 hours (changed every 6 hours). The so obtained keratin solution was then centrifuged twice (5 C, 9000 rpm, 20 min per cycle) to remove insoluble particles, resulting in a clear protein solution ( wt%), which was then concentrated to 2 wt% through a centrifugal evaporator. The total extraction yield was 47 5%. Film Preparation and slow drying process: Keratin films were fabricated by solvent casting keratin solution on PDMS molds. Slow drying process was achieved by controlling the relative humidity environment (RH=30-95%) during keratin solution solvent casting by using a custom made humidity chamber. Diffractive PDMS mold and PDMS-made multi-lens arrays were fabricated using optical diffraction gratings (Edmund Optics, lines/mm) 2

3 or optical cards (Digital Optics Corp., Tessera Technologies Inc.) as masters. After drying, films were let acclimated to RH=30% and then carefully lifted from the mold. Film thickness was controlled by varying either keratin concentration or solution volume used during casting. Inverse opal fabrication: PMMA nanospheres ( =250 nm) were used to fabricate an opal template (1% concentration dispersed in water, Phosphorex). The PMMA solution was deposited onto a silicon wafer, which was then heated on a hotplate at 90 C to generate the PMMA opal by self-assembly induced by water evaporation. The keratin solution was then added to the PMMA opal and filled the air voids by capillary infiltration. The solution was set to dry in a film at room temperature and RH=95%. The so formed keratin film was soaked in acetone for 24 h to allow for detachment from the silicon wafer and removal of the PMMA nanospheres. Measurement of regenerated keratin molecular weight and purity: Cashmere-derived keratin was diluted 1:1 with a solution of 2x Laemmli sample buffer, 4% SDS, 20% glycerol, 10% 2- mercaptoethanol and M Tris HCl. Keratins were then run in a vertical slab gel electrophoretic system at 200 V, 80 ma, and 25W. A solution of 0.1% Coomassie brilliant blue R-250 (Sigma),10% acetic acid, and 40% methanol was then used to stain the keratin in the gel for 1 h. Excess of staining was then removed by rinsing the gel in deionized water overnight. Physical characterization: Scanning electron microscopy (SEM) was used to investigate keratin film morphology and to determine surface patterning. Casted films were mounted on carbon tape and sputter coated with platinum-palladium. The films were then imaged using a scanning electron microscope (Supra55VP, Zeiss). Atomic force microscopy (AFM) was used to investigate surface morphology and to determine surface roughness of non-patterned and patterned keratin films. Micrographs of keratin films were acquired with a Digital Instrument Dimension 3100 (Veeco Instruments, Inc.) in tapping mode. Keratin film spectrum 3

4 in the visible wavelengths was measured with a USB2000 Miniature Fiber Optic Spectrometer. A Metricon waveguide instrument was used to evaluate refractive index of keratin films. The measured indices of refraction and film thicknesses are evaluated at a wavelength of λ = 633 nm, as previously reported for silk fibroin. Spectroscopical characterization: Attenuated Total Reflectance Fourier Transform Infrared (ATR-FTIR) spectroscopy of keratin films was performed with a Jasco FT/IR-6200 Spectrometer, equipped with a multiple reflection, horizontal MIRacle attachment (Ge crystal, from Pike Tech., Madison, WI). Each collected spectrum was obtained as an average of 128 scans with a wavenumber range of cm -1 and a nominal resolution of 4 cm -1. To analyze keratin conformational changes as a function of slow drying processing, Amide I and Amide III peak absorptions were analyzed as previously reported 2, 3. Micro-Raman spectroscopy was performed with a Jasco NRS-3000 spectrometer in the cm -1 range using a 733 laser and a 100x objective. Each spectra was collected as an average of 20 scans (10s per scan) with a resolution of 1 cm -1. Cosmic rays removal, measurement of FWHM and of I 850 /I 830 ratio were performed with Jasco Spectra Analysis software. Ellman s reagent was used to determine the content of free thiol groups of cysteine residues in the cashmere-derived regenerated keratin solution and in assembled films 4. References 1. A. Nakamura, M. Arimoto, K. Takeuchi and T. Fujii, Biological and Pharmaceutical Bulletin, 2002, 25, A. Vasconcelos, G. Freddi and A. Cavaco-Paulo, Biomacromolecules, 2008, 9, G. Freddi, G. Pessina and M. Tsukada, International Journal of Biological Macromolecules, 1999, 24, G. L. Ellman, Archives of Biochemistry and Biophysics, 1959, 82,

5 Table S1. Reduced cysteine content (measured as free thiol group through Ellman s reagent assay) in cashmere-derived regenerated keratin solution, in keratin films assembled at increasing relative humidity values, and in keratin films after acetone post-treatment Keratin material Free thiol group concentration [slow-drying relative humidity, %] [mm] Keratin solution 0.976±0.231 Film [RH=50%] 0.061±0.018 Film [RH=75%] 0.143±0.041 Film [RH=95%] 0.579±0.074 Film [RH=95%] Acetone post-treatment 0.302±

6 Figure S1 Figure S1. SDS-PAGE of standard protein molecular weight markers (left lane) and cashmere-extracted keratin (right lane). 6

7 Figure S2 Figure S2. Photograph of projected patterns obtained from propagation of a green light laser source through keratin-made 2D diffractive phase masks. The images are taken at a distance of 10 cm from the keratin optical element. (Master from Digital Optics Inc., Tessera Corporation). 7

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